Allosteric modulation of cytochrome P450 enzymes by the NADPH cytochrome P450 reductase FMN-containing domain
Author:
Funder
National Institutes of Health
NIGMS
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference76 articles.
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4. NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family;Iyanagi;Arch. Biochem. Biophys.,2012
5. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes;Wang;Proc. Natl. Acad. Sci. U. S. A.,1997
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1. Decoding the Role of CYP450 Enzymes in Metabolism and Disease: A Comprehensive Review;Biomedicines;2024-07-02
2. Structural insights into the semiquinone form of human Cytochrome P450 reductase by DEER distance measurements between a native flavin and a spin labelled non‐canonical amino acid;Chemistry – A European Journal;2024-02-13
3. Discovery of tricyclic PARP7 inhibitors with high potency, selectivity, and oral bioavailability;European Journal of Medicinal Chemistry;2024-02
4. Allosteric modulation of cytochrome P450 enzymes by the NADPH cytochrome P450 reductase FMN-containing domain;Journal of Biological Chemistry;2023-09
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